ArticlePloS one2015
Computational study of a model system of enzyme-mediated [4+2] cycloaddition reaction.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Conceptual similarities between zeolites and artificial enzymes.Chemical science · 2019Article
- Influence of water and enzyme SpnF on the dynamics and energetics of the ambimodal [6+4]/[4+2] cycloaddition.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Computational Insights into an Enzyme-Catalyzed [4+2] Cycloaddition.The Journal of organic chemistry · 2017Article
- Investigation of the mechanism of the SpnF-catalyzed [4+2]-cycloaddition reaction in the biosynthesis of spinosyn A.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Natural [4 + 2]-Cyclases.Chemical reviews · 2017Review
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Authors and funding
2 authors.
Funding
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Abstract
A possible mechanistic pathway related to an enzyme-catalyzed [4+2] cycloaddition reaction was studied by theoretical calculations at density functional (B3LYP, O3LYP, M062X) and semiempirical levels (PM6-DH2, PM6) performed on a model system. The calculations were carried out for the key [4+2] cycloaddition step considering enzyme-catalyzed biosynthesis of Spinosyn A in a model reaction, where a reliable example of a biological Diels-Alder reaction was reported experimentally. In the present study it was demonstrated that the [4+2] cycloaddition reaction may benefit from moving along the energetically balanced reaction coordinate, which enabled the catalytic rate enhancement of the [4+2] cycloaddition pathway involving a single transition state. Modeling of such a system with coordination of three amino acids indicated a reliable decrease of activation energy by ~18.0 kcal/mol as compared to a non-catalytic transformation.
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